Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxiredoxin-1

Gene

Prdx1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei52Cysteine sulfenic acid (-SOH) intermediate1

GO - Molecular functioni

  • heme binding Source: RGD
  • peroxidase activity Source: UniProtKB-KW
  • peroxiredoxin activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • response to oxidative stress Source: RGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4508. Rno2CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-1 (EC:1.11.1.15)
Alternative name(s):
HBP23
Heme-binding 23 kDa protein
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene namesi
Name:Prdx1
Synonyms:Tdpx2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620039. Prdx1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001350782 – 199Peroxiredoxin-1Add BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei7N6-acetyllysine; alternateBy similarity1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei27N6-acetyllysineBy similarity1
Modified residuei32PhosphoserineBy similarity1
Modified residuei35N6-acetyllysine; alternateBy similarity1
Modified residuei35N6-succinyllysine; alternateBy similarity1
Disulfide bondi52Interchain (with C-173); in linked formCombined sources2 Publications
Modified residuei90PhosphothreonineBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei136N6-acetyllysineBy similarity1
Disulfide bondi173Interchain (with C-52); in linked formCombined sources2 Publications
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylated on Thr-90 during the M-phase, which leads to a decrease in enzymatic activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63716.
PRIDEiQ63716.

2D gel databases

World-2DPAGEi0004:Q63716.

PTM databases

iPTMnetiQ63716.
PhosphoSitePlusiQ63716.
SwissPalmiQ63716.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017194.
GenevisibleiQ63716. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (PubMed:10535922). 5 homodimers assemble to form a ring-like decamer (PubMed:17974571). Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts with SESN1 and SESN2 (By similarity).By similarity2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi250701. 3 interactors.
IntActiQ63716. 5 interactors.
STRINGi10116.ENSRNOP00000023132.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 20Combined sources5
Beta strandi26 – 30Combined sources5
Helixi31 – 34Combined sources4
Beta strandi37 – 43Combined sources7
Beta strandi50 – 52Combined sources3
Helixi57 – 61Combined sources5
Helixi63 – 68Combined sources6
Beta strandi71 – 78Combined sources8
Helixi81 – 88Combined sources8
Helixi92 – 94Combined sources3
Beta strandi104 – 106Combined sources3
Helixi111 – 115Combined sources5
Beta strandi121 – 124Combined sources4
Beta strandi128 – 133Combined sources6
Beta strandi137 – 145Combined sources9
Helixi153 – 168Combined sources16
Beta strandi170 – 172Combined sources3
Turni188 – 191Combined sources4
Helixi192 – 195Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QQ2X-ray2.60A/B1-199[»]
2Z9SX-ray2.90A/B/C/D/E/F/G/H/I/J1-199[»]
ProteinModelPortaliQ63716.
SMRiQ63716.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63716.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 165ThioredoxinPROSITE-ProRule annotationAdd BLAST160

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ63716.
KOiK13279.
OMAiFAWTNTP.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ63716.
TreeFamiTF105181.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR036249. Thioredoxin-like_sf.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM
110 120 130 140 150
NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG
160 170 180 190
RSVDEILRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK
Length:199
Mass (Da):22,109
Last modified:November 1, 1996 - v1
Checksum:iBDF2D4ABA8A776DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.
PIRiI52425.
RefSeqiNP_476455.1. NM_057114.1.
UniGeneiRn.2845.

Genome annotation databases

EnsembliENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
GeneIDi117254.
KEGGirno:117254.
UCSCiRGD:620039. rat.

Similar proteinsi

Entry informationi

Entry nameiPRDX1_RAT
AccessioniPrimary (citable) accession number: Q63716
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 25, 2017
This is version 149 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families